P22204 (DBF2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cell cycle protein kinase DBF2
EC=2.7.11.1

Gene names

Name:	DBF2
Ordered Locus Names:	YGR092W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	572 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Is probably a Ser/Thr-protein kinase that may function in initiation of DNA synthesis and also in late nuclear division.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Phosphorylation inactivates the enzyme Potential.
Induction	Is periodically expressed in the cell-cycle, probably near the start phase of the cycle.
Miscellaneous	Present with 3500 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 AGC-kinase C-terminal domain. Contains 1 protein kinase domain.
Sequence caution	The sequence AAA34559.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell cycle
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW nuclear division Inferred from mutant phenotype Ref.1. Source: SGD vacuolar acidification Inferred from mutant phenotype. Source: SGD
Cellular component	cellular bud neck Inferred from direct assay. Source: SGD spindle pole body Inferred from direct assay. Source: SGD vacuole Inferred from mutant phenotype. Source: GOC
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MOB1	P40484	6	EBI-5569,EBI-11119

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 572	572	Cell cycle protein kinase DBF2		PRO_0000085918
Regions
	Domain	177 – 477	301	Protein kinase
	Domain	478 – 555	78	AGC-kinase C-terminal
	Nucleotide binding	183 – 191	9	ATP By similarity
Sites
	Active site	300	1	Proton acceptor By similarity
	Binding site	206	1	ATP By similarity
Amino acid modifications
	Modified residue	83	1	Phosphoserine By similarity
	Modified residue	188	1	Phosphotyrosine By similarity
	Modified residue	374	1	Phosphoserine Ref.7 Ref.8
	Modified residue	544	1	Phosphothreonine Ref.6
Experimental info
	Sequence conflict	11 – 12	2	LL → HM Ref.1
	Sequence conflict	114	1	H → Y in AAA34559. Ref.1
	Sequence conflict	246	1	D → E in AAA34559. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P22204 [UniParc]. Last modified October 1, 1996. Version 3. Checksum: 648C565D5CE7117D	FASTA	572	66,148
	10 20 30 40 50 60 MLSKSEKNVD LLAGNMSNLS FDGHGTPGGT GLFPNQNITK RRTRPAGIND SPSPVKPSFF 70 80 90 100 110 120 PYEDTSNMDI DEVSQPDMDV SNSPKKLPPK FYERATSNKT QRVVSVCKMY FLEHYCDMFD 130 140 150 160 170 180 YVISRRQRTK QVLEYLQQQS QLPNSDQIKL NEEWSSYLQR EHQVLRKRRL KPKNRDFEMI 190 200 210 220 230 240 TQVGQGGYGQ VYLARKKDTK EVCALKILNK KLLFKLNETK HVLTERDILT TTRSEWLVKL 250 260 270 280 290 300 LYAFQDLQSL YLAMEFVPGG DFRTLLINTR CLKSGHARFY ISEMFCAVNA LHDLGYTHRD 310 320 330 340 350 360 LKPENFLIDA KGHIKLTDFG LAAGTISNER IESMKIRLEK IKDLEFPAFT EKSIEDRRKM 370 380 390 400 410 420 YNQLREKEIN YANSMVGSPD YMALEVLEGK KYDFTVDYWS LGCMLFESLV GYTPFSGSST 430 440 450 460 470 480 NETYDNLRRW KQTLRRPRQS DGRAAFSDRT WDLITRLIAD PINRLRSFEH VKRMSYFADI 490 500 510 520 530 540 NFSTLRSMIP PFTPQLDSET DAGYFDDFTS EADMAKYADV FKRQDKLTAM VDDSAVSSKL 550 560 570 VGFTFRHRNG KQGSSGILFN GLEHSDPFST FY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The product of the Saccharomyces cerevisiae cell cycle gene DBF2 has homology with protein kinases and is periodically expressed in the cell cycle." Johnston L.H., Eberly S.L., Chapman J.W., Araki H., Sugino A. Mol. Cell. Biol. 10:1358-1366(1990) [PubMed: 2181271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The cell-cycle-regulated budding yeast gene DBF2, encoding a putative protein kinase, has a homologue that is not under cell-cycle control." Toyn J.H., Araki H., Sugino A., Johnston L.H. Gene 104:63-70(1991) [PubMed: 1916278] [Abstract] Cited for: SEQUENCE REVISION TO N-TERMINUS.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-544, MASS SPECTROMETRY. Strain: YAL6B.
[7]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, MASS SPECTROMETRY.
[8]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M34146 Genomic DNA. Translation: AAA34559.1. Different initiation. Z72877 Genomic DNA. Translation: CAA97095.1. BK006941 Genomic DNA. Translation: DAA08185.1.
PIR	S64387.
RefSeq	NP_011606.1. NM_001181221.1.
3D structure databases
ProteinModelPortal	P22204.
SMR	P22204. Positions 166-547.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2319N.
IntAct	P22204. 42 interactions.
MINT	MINT-517674.
STRING	P22204.
Proteomic databases
PeptideAtlas	P22204.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGR092W; YGR092W; YGR092W.
GeneID	852984.
KEGG	sce:YGR092W.
NMPDR	fig|4932.3.peg.2723.
Organism-specific databases
CYGD	YGR092w.
SGD	S000003324. DBF2.
Phylogenomic databases
eggNOG	fuNOG04073.
GeneTree	EFGT00070000008712.
HOGENOM	HBG396340.
OMA	GTISNER.
OrthoDB	EOG43XZC4.
Enzyme and pathway databases
BRENDA	2.7.11.1. 984.
Gene expression databases
ArrayExpress	P22204.
Genevestigator	P22204.
GermOnline	YGR092W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011009. Kinase-like_dom. IPR017892. Pkinase_C. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K06684.
Pfam	PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
SMART	SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	972797.

Entry information

Entry name

DBF2_YEAST

Accession

Primary (citable) accession number: P22204
Secondary accession number(s): D6VUM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	October 1, 1996
Last modified:	December 14, 2011
This is version 114 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program